Publication: Comparison of accessible surface area solvent models inpredicting the native structure of Met-enkephalin

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Title	Comparison of accessible surface area solvent models inpredicting the native structure of Met-enkephalin
Authors/Editors*	Lixin Zhan, Jeff Z. Y. Chen, and Wing-Ki Liu
Where published*	In preparation
How published*	Journal
Year*	2007
Volume	-1
Number	-1
Pages
Publisher
Keywords
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Abstract	In this paper, we assess the influence of different accessible surface area solvent models to the global minimum structures of proteins/peptides. Met-enkephalin was adopted as the model peptide with simulations performed based on ECEPP/2 and ECEPP/3 force fields. The global minima and their corresponding conformations were obtained. By comparing the global minimum structures, we analyzed the effect introduced by using different solvent models. The results suggest that implicit solvent models should be employed in simulations with caution. Further examinations for their reliability are required. Simulations {\it in vacuo} are still choices for conformational studies. Further, the influence of fixing the peptide angles $\omega$ were examined. Obvious conformational variances were noticed when $\omega$ were fixed at $180^\circ$.